Thermal activation of photoactivatable urocanase from Pseudomonas putida
The dark inactivation of urocanase from Pseudomonas putida is caused by the formation of a sulfite adduct of the tightly bound coenzyme, nicotinamide adenine dinucleotide. Photodissociation of this adduct by UV radiation restores the enzyme activity. Based on cold exhaustive dialysis the modificatio...
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| Veröffentlicht in: | Journal of photochemistry and photobiology. B, Biology Biology, 1989-06, Vol.3 (3), p.429-435 |
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| container_title | Journal of photochemistry and photobiology. B, Biology |
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| creator | O'Donnell, Peter S. Hug, Daniel H. |
| description | The dark inactivation of urocanase from
Pseudomonas putida is caused by the formation of a sulfite adduct of the tightly bound coenzyme, nicotinamide adenine dinucleotide. Photodissociation of this adduct by UV radiation restores the enzyme activity. Based on cold exhaustive dialysis the modification reaction appeared to be irreversible. However, we now report that sulfite modification of urocanase is reversible at higher temperatures. An Arrhenius plot of the thermal activation is linear (20–38 °C). The activation energy for the enzyme activation is 114 kJ mol
−1. The substance that is photodissociated from inactive urocanase reacts with urocanase to reform the modified enzyme indicating that sulfite is not oxidized, or otherwise changed through these processes. Nucleophiles (sulfite, hydroxylamine, hydride, cyanide) are known to inhibit urocanase by forming adducts with nicotinamide adenine dinucleotide. Urocanase inactivated by hydride or cyanide is not reactivated thermally or photochemically. Urocanase inactivated by hydroxylamine and by glycylglycine can be reactivated by a thermal reaction. In conclusion, sulfite-modified urocanase, which is formed in cells, can be reactivated not only by sunlight but also at physiological temperatures. |
| doi_str_mv | 10.1016/1011-1344(89)80047-8 |
| format | Article |
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Pseudomonas putida is caused by the formation of a sulfite adduct of the tightly bound coenzyme, nicotinamide adenine dinucleotide. Photodissociation of this adduct by UV radiation restores the enzyme activity. Based on cold exhaustive dialysis the modification reaction appeared to be irreversible. However, we now report that sulfite modification of urocanase is reversible at higher temperatures. An Arrhenius plot of the thermal activation is linear (20–38 °C). The activation energy for the enzyme activation is 114 kJ mol
−1. The substance that is photodissociated from inactive urocanase reacts with urocanase to reform the modified enzyme indicating that sulfite is not oxidized, or otherwise changed through these processes. Nucleophiles (sulfite, hydroxylamine, hydride, cyanide) are known to inhibit urocanase by forming adducts with nicotinamide adenine dinucleotide. Urocanase inactivated by hydride or cyanide is not reactivated thermally or photochemically. Urocanase inactivated by hydroxylamine and by glycylglycine can be reactivated by a thermal reaction. In conclusion, sulfite-modified urocanase, which is formed in cells, can be reactivated not only by sunlight but also at physiological temperatures.</description><identifier>ISSN: 1011-1344</identifier><identifier>EISSN: 1873-2682</identifier><identifier>DOI: 10.1016/1011-1344(89)80047-8</identifier><identifier>PMID: 2570140</identifier><identifier>CODEN: JPPBEG</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>activation energy ; Biological and medical sciences ; Biological effects of radiation ; Enzyme Activation ; Fundamental and applied biological sciences. Psychology ; glycylglycine ; Hot Temperature ; Hydro-Lyases - metabolism ; hydroxylamine ; Light ; Photoactivation ; Photochemistry ; Pseudomonas - enzymology ; Pseudomonas putida ; Radiosensitizing agents. Photosensitizing agents. Thermosensitizing agents ; sulfite ; Sulfites - metabolism ; thermal activation ; Tissues, organs and organisms biophysics ; Ultraviolet Rays ; urocanase ; Urocanate Hydratase - antagonists & inhibitors ; Urocanate Hydratase - metabolism</subject><ispartof>Journal of photochemistry and photobiology. B, Biology, 1989-06, Vol.3 (3), p.429-435</ispartof><rights>1989</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-cc5f9287bc90435eef1a60629af6487b698d8b766f45ea07aa2ba538cf80fa9f3</citedby><cites>FETCH-LOGICAL-c386t-cc5f9287bc90435eef1a60629af6487b698d8b766f45ea07aa2ba538cf80fa9f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/1011-1344(89)80047-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6860638$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2570140$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>O'Donnell, Peter S.</creatorcontrib><creatorcontrib>Hug, Daniel H.</creatorcontrib><title>Thermal activation of photoactivatable urocanase from Pseudomonas putida</title><title>Journal of photochemistry and photobiology. B, Biology</title><addtitle>J Photochem Photobiol B</addtitle><description>The dark inactivation of urocanase from
Pseudomonas putida is caused by the formation of a sulfite adduct of the tightly bound coenzyme, nicotinamide adenine dinucleotide. Photodissociation of this adduct by UV radiation restores the enzyme activity. Based on cold exhaustive dialysis the modification reaction appeared to be irreversible. However, we now report that sulfite modification of urocanase is reversible at higher temperatures. An Arrhenius plot of the thermal activation is linear (20–38 °C). The activation energy for the enzyme activation is 114 kJ mol
−1. The substance that is photodissociated from inactive urocanase reacts with urocanase to reform the modified enzyme indicating that sulfite is not oxidized, or otherwise changed through these processes. Nucleophiles (sulfite, hydroxylamine, hydride, cyanide) are known to inhibit urocanase by forming adducts with nicotinamide adenine dinucleotide. Urocanase inactivated by hydride or cyanide is not reactivated thermally or photochemically. Urocanase inactivated by hydroxylamine and by glycylglycine can be reactivated by a thermal reaction. In conclusion, sulfite-modified urocanase, which is formed in cells, can be reactivated not only by sunlight but also at physiological temperatures.</description><subject>activation energy</subject><subject>Biological and medical sciences</subject><subject>Biological effects of radiation</subject><subject>Enzyme Activation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>glycylglycine</subject><subject>Hot Temperature</subject><subject>Hydro-Lyases - metabolism</subject><subject>hydroxylamine</subject><subject>Light</subject><subject>Photoactivation</subject><subject>Photochemistry</subject><subject>Pseudomonas - enzymology</subject><subject>Pseudomonas putida</subject><subject>Radiosensitizing agents. Photosensitizing agents. Thermosensitizing agents</subject><subject>sulfite</subject><subject>Sulfites - metabolism</subject><subject>thermal activation</subject><subject>Tissues, organs and organisms biophysics</subject><subject>Ultraviolet Rays</subject><subject>urocanase</subject><subject>Urocanate Hydratase - antagonists & inhibitors</subject><subject>Urocanate Hydratase - metabolism</subject><issn>1011-1344</issn><issn>1873-2682</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLxTAQhYMovv-BQhciuqgmbZqkG0EuvkDQha7DNJ1gpG2uSSv47831VpdmMRnOfHNIDiFHjF4wysRlKixnJednqj5XlHKZqw2yy5Qs80KoYjP1v8gO2YvxnaZTCblNtotKUsbpLrl_ecPQQ5eBGd0njM4PmbfZ8s2Pfpag6TCbgjcwQMTMBt9nzxGn1vc-KdlyGl0LB2TLQhfxcL73yevtzcviPn98untYXD_mplRizI2pbF0o2Zia8rJCtAwEFUUNVvAki1q1qpFCWF4hUAlQNFCVylhFLdS23Cena99l8B8TxlH3LhrsOhjQT1HLmknFyyKBfA2a4GMMaPUyuB7Cl2ZUrwJcFaZX6WhV658AtUprx7P_1PTY_i3NiaX5yTyHaKCzAQbj4h8mVPpNubK5WmOYsvh0GHQ0DgeDrQtoRt169_87vgFohozU</recordid><startdate>19890601</startdate><enddate>19890601</enddate><creator>O'Donnell, Peter S.</creator><creator>Hug, Daniel H.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19890601</creationdate><title>Thermal activation of photoactivatable urocanase from Pseudomonas putida</title><author>O'Donnell, Peter S. ; Hug, Daniel H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-cc5f9287bc90435eef1a60629af6487b698d8b766f45ea07aa2ba538cf80fa9f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>activation energy</topic><topic>Biological and medical sciences</topic><topic>Biological effects of radiation</topic><topic>Enzyme Activation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>glycylglycine</topic><topic>Hot Temperature</topic><topic>Hydro-Lyases - metabolism</topic><topic>hydroxylamine</topic><topic>Light</topic><topic>Photoactivation</topic><topic>Photochemistry</topic><topic>Pseudomonas - enzymology</topic><topic>Pseudomonas putida</topic><topic>Radiosensitizing agents. Photosensitizing agents. Thermosensitizing agents</topic><topic>sulfite</topic><topic>Sulfites - metabolism</topic><topic>thermal activation</topic><topic>Tissues, organs and organisms biophysics</topic><topic>Ultraviolet Rays</topic><topic>urocanase</topic><topic>Urocanate Hydratase - antagonists & inhibitors</topic><topic>Urocanate Hydratase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>O'Donnell, Peter S.</creatorcontrib><creatorcontrib>Hug, Daniel H.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of photochemistry and photobiology. B, Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>O'Donnell, Peter S.</au><au>Hug, Daniel H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thermal activation of photoactivatable urocanase from Pseudomonas putida</atitle><jtitle>Journal of photochemistry and photobiology. B, Biology</jtitle><addtitle>J Photochem Photobiol B</addtitle><date>1989-06-01</date><risdate>1989</risdate><volume>3</volume><issue>3</issue><spage>429</spage><epage>435</epage><pages>429-435</pages><issn>1011-1344</issn><eissn>1873-2682</eissn><coden>JPPBEG</coden><abstract>The dark inactivation of urocanase from
Pseudomonas putida is caused by the formation of a sulfite adduct of the tightly bound coenzyme, nicotinamide adenine dinucleotide. Photodissociation of this adduct by UV radiation restores the enzyme activity. Based on cold exhaustive dialysis the modification reaction appeared to be irreversible. However, we now report that sulfite modification of urocanase is reversible at higher temperatures. An Arrhenius plot of the thermal activation is linear (20–38 °C). The activation energy for the enzyme activation is 114 kJ mol
−1. The substance that is photodissociated from inactive urocanase reacts with urocanase to reform the modified enzyme indicating that sulfite is not oxidized, or otherwise changed through these processes. Nucleophiles (sulfite, hydroxylamine, hydride, cyanide) are known to inhibit urocanase by forming adducts with nicotinamide adenine dinucleotide. Urocanase inactivated by hydride or cyanide is not reactivated thermally or photochemically. Urocanase inactivated by hydroxylamine and by glycylglycine can be reactivated by a thermal reaction. In conclusion, sulfite-modified urocanase, which is formed in cells, can be reactivated not only by sunlight but also at physiological temperatures.</abstract><cop>Lausanne</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>2570140</pmid><doi>10.1016/1011-1344(89)80047-8</doi><tpages>7</tpages></addata></record> |
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| ispartof | Journal of photochemistry and photobiology. B, Biology, 1989-06, Vol.3 (3), p.429-435 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | activation energy Biological and medical sciences Biological effects of radiation Enzyme Activation Fundamental and applied biological sciences. Psychology glycylglycine Hot Temperature Hydro-Lyases - metabolism hydroxylamine Light Photoactivation Photochemistry Pseudomonas - enzymology Pseudomonas putida Radiosensitizing agents. Photosensitizing agents. Thermosensitizing agents sulfite Sulfites - metabolism thermal activation Tissues, organs and organisms biophysics Ultraviolet Rays urocanase Urocanate Hydratase - antagonists & inhibitors Urocanate Hydratase - metabolism |
| title | Thermal activation of photoactivatable urocanase from Pseudomonas putida |
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